ArticleNucleic acids research2021
The human pseudouridine synthase PUS7 recognizes RNA with an extended multi-domain binding surface.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Reduced sensitivity to RNA structural differences distinguishes eukaryotic Pus4 from bacterial TruB.RNA (New York, N.Y.) · 2026Article
- In silico analysis of gene expression signatures and drug repurposing associated with metastatic progression in melanoma (skin cancer).Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- The impact of psuedouridine modification on human tRNA.Biochemical Society transactions · 2026Review
- Pseudouridine synthase 7 as a context-specific therapeutic target in cancer.The Journal of pharmacology and experimental therapeutics · 2026Review
- Cytoplasmic localization of pseudouridine synthase 7 facilitates a pseudouridine-dependent enhancement of cellular stress tolerance.Nature communications · 2026Article
- Quantitative analysis of small RNA pseudouridylation reveals interplay of PUS enzymes in tRNA anticodon stem-loop.Nature communications · 2026Article
- Integrative analysis of nanopore direct RNA sequencing data reveals a global impact of pseudouridylation on mNPJ precision oncology · 2026Article
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- tRNA modifications: greasing the wheels of translation and beyond.RNA biology · 2025Review
- Advances in RNA modification in myocardial fibrosis (Review).International journal of molecular medicine · 2025Review
- RNA modifications in health and disease: from mechanistic insights to therapeutic applications.Precision clinical medicine · 2025Review
- Nano-Mod-Amp reveals RNA sequence, structural and cell type specific features of pseudouridylation by PUS7.bioRxiv : the preprint server for biology · 2025Article
- Pseudouridylation of 7SK by PUS7 regulates Pol II transcription elongation.Nature communications · 2025Article
- Cytoplasmic localization of PUS7 facilitates a pseudouridine-dependent enhancement of cellular stress tolerance.bioRxiv : the preprint server for biology · 2025Article
- Review
- MoDorado: enhanced detection of tRNA modifications in nanopore sequencing by off-label use of modification callers.Nucleic acids research · 2025Article
- Determining the effects of pseudouridine incorporation on human tRNAs.The EMBO journal · 2025Article
- tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025Article
- Identification and Characterization of the RNA Modifying Factors PUS7 and WTAP as Key Components for the Control of Tumor Biological Processes in Renal Cell Carcinomas.Current issues in molecular biology · 2025Article
- Identification of RNA processing factor LSM5 as a new adverse biomarker in nasopharyngeal carcinoma.Scientific reports · 2025Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human pseudouridine synthase PUS7 is a versatile RNA modification enzyme targeting many RNAs thereby playing a critical role in development and brain function. Whereas all target RNAs of PUS7 share a consensus sequence, additional recognition elements are likely required, and the structural basis for RNA binding by PUS7 is unknown. Here, we characterize the structure-function relationship of human PUS7 reporting its X-ray crystal structure at 2.26 Å resolution. Compared to its bacterial homolog, human PUS7 possesses two additional subdomains, and structural modeling studies suggest that these subdomains contribute to tRNA recognition through increased interactions along the tRNA substrate. Consistent with our modeling, we find that all structural elements of tRNA are required for productive interaction with PUS7 as the consensus sequence of target RNA alone is not sufficient for pseudouridylation by human PUS7. Moreover, PUS7 binds several, non-modifiable RNAs with medium affinity which likely enables PUS7 to screen for productive RNA substrates. Following tRNA modification, the product tRNA has a significantly lower affinity for PUS7 facilitating its dissociation. Taken together our studies suggest a combination of structure-specific and sequence-specific RNA recognition by PUS7 and provide mechanistic insight into its function.
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